Recombinant monoclonal antibodies and Fc-fusion proteins have become an important class of biological pharmaceuticals and research reagents. Their manufacture typically involves mammalian cells as the expression host and affinity chromatography as a key purification step. While upstream processes such as cell-line development and engineering have significantly enhanced antibody yields, the downstream purification steps remain expensive and reduce productivity. The vast majority of antibody purification pipelines employ a Protein A-based purification step, which contributes to the majority of the raw-material costs1, 2. Antibody elution from a Protein A column is typically achieved by lowering the pH to 3. However, at such low pH, aggregation and denaturation of the antibody and of Fc-fusion proteins can easily occur.